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Yeast Porphobilinogen Deaminase also Forms Enzyme-Pyrrole Intermediates
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The enzyme porphobilinogen deaminase (PBG deaminase. EC 4.3.1.8) catalyzes
the condensation of four molecules of PBG to give the linear tetrapyrrol, hydroxymethylbilane.
It has been shown that this enzyme forms stable mono-, di-, tri- and tetrapyrrol-
enzyme covalent complexes. When the enzyme, partially purified in the absence or
presence of phenylmethylsulfonyl fluoride (PMSF) and preincubated with PBG. was applied
on DEAE-cellulose columns, three peaks with PBG deaminase activity were detected.
Using Ehrlich’s reagent, it was found that the active peaks corresponded to
mono-, di- and tri-pyrrylmethane-enzyme complexes. Therefore, the mechanism of action
of PBG deaminase from Saccharomyces cerevisiae also involves the sequential addition
of four PBG units, leading to the formation of the enzyme-substrate intermediate
complexes, as has already been described for the same enzyme from other sources.
Title: Yeast Porphobilinogen Deaminase also
Forms Enzyme-Pyrrole Intermediates
Description:
The enzyme porphobilinogen deaminase (PBG deaminase.
EC 4.
3.
1.
8) catalyzes
the condensation of four molecules of PBG to give the linear tetrapyrrol, hydroxymethylbilane.
It has been shown that this enzyme forms stable mono-, di-, tri- and tetrapyrrol-
enzyme covalent complexes.
When the enzyme, partially purified in the absence or
presence of phenylmethylsulfonyl fluoride (PMSF) and preincubated with PBG.
was applied
on DEAE-cellulose columns, three peaks with PBG deaminase activity were detected.
Using Ehrlich’s reagent, it was found that the active peaks corresponded to
mono-, di- and tri-pyrrylmethane-enzyme complexes.
Therefore, the mechanism of action
of PBG deaminase from Saccharomyces cerevisiae also involves the sequential addition
of four PBG units, leading to the formation of the enzyme-substrate intermediate
complexes, as has already been described for the same enzyme from other sources.
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